Aortic Ductus Diverticulum Mimicking Aortic Dissection: A Case of Diagnostic Ambiguity in Transthoracic Echocardiography.

Background: Aortic dissection is a critical condition often presenting with acute, severe chest pain and haemodynamic instability. Early diagnosis is essential to mitigate the high mortality risk. Imaging modalities play a pivotal role in diagnosing aortic conditions, but determining the appropriate method can be challenging.

The multifunctional GIT family of proteins.

The G-protein-coupled receptor (GPCR)-kinase-interacting proteins 1 and 2 (GIT1 and GIT2) are ubiquitous multidomain proteins involved in diverse cellular processes. They traffic between three distinct cellular compartments (cytoplasmic complexes, focal adhesions and the cell periphery) through interactions with proteins including ARF, Rac1 and Cdc42 GTPases, p21-activated kinase (PAK), PAK-interacting exchange factor (PIX), the kinase MEK1, phospholipase Cgamma (PLCgamma) and paxillin. GITs and PIX cooperate to form large oligomeric complexes to which other proteins are transiently recruited.

GIT1 mediates thrombin signaling in endothelial cells: role in turnover of RhoA-type focal adhesions.

Thrombin mediates changes in endothelial barrier function and increases endothelial permeability. A feature of thrombin-enhanced endothelial hyperpermeability is contraction of endothelial cells (ECs), accompanied by formation of focal adhesions (FAs). Recently, a G protein-coupled receptor kinase-interacting protein, GIT1, was shown to regulate FA disassembly.

The role of MAP kinases in endothelial activation.

Activation of endothelial cells by proinflammatory stimuli results in increased migration of leukocytes across the endothelium, which contributes to the progression of atherosclerosis. Thus, control of the inflammatory status of endothelial cells, which is achieved by a balance of pro- and antiinflammatory signals, is crucial to limiting the disease. The mitogen-activated protein kinases (MAPKs) are a family of central signaling molecules that respond to numerous stimuli by phosphorylating a variety of substrates including transcription factors, enzymes, and other kinases.

Fluid shear stress attenuates hydrogen peroxide-induced c-Jun NH2-terminal kinase activation via a glutathione reductase-mediated mechanism.

c-Jun NH2-terminal kinase (JNK) is activated by a number of cellular stimuli including reactive oxygen species (ROS). Previous studies have demonstrated that fluid shear stress (flow) inhibits cytokine-induced JNK activation in endothelial cells (ECs). In the present study, we show JNK activation by ROS in ECs and hypothesized that flow inhibits ROS-induced JNK activation in ECs via modulation of cellular protection systems against ROS.